ID A0A0D2BD07_9EURO Unreviewed; 2238 AA.
AC A0A0D2BD07;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Pre-mRNA-splicing factor brr2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_04043 {ECO:0000313|EMBL:KIW16853.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16853.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW16853.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16853.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847494; KIW16853.1; -; Genomic_DNA.
DR RefSeq; XP_016237069.1; XM_016378392.1.
DR STRING; 91928.A0A0D2BD07; -.
DR GeneID; 27331126; -.
DR VEuPathDB; FungiDB:PV08_04043; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 543..727
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 766..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1394..1570
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 50..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2101..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2111..2126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2238 AA; 251967 MW; 2E1D313267E288AD CRC64;
MADQNISQYK YSAMSNLVLQ ADRRLYSRNK DENTGDPESL AGRLNIRDMG SRVAREQAPK
PKKMAPGLGM ERGTIHEGED VLERERRKRK RGEPAQTRGA GILSAGDALI EGLKYRPRTP
ATRATYDLLL TVTANALGDV SQEIVRSAAD AILEFLKDDN MKDLDKKKEV DEIVGTTMTP
KEFNELVNLG KKITDYDAQD EDEDMADGDE AELDDRQGVA VVFDEDDEDE DGIARTYEVR
DEDEDSDEED DIQDQPDDEA ATAGGAGAPD IDPDDEDTGM VLDSGIADSS RRKREDSDLV
PIHEIDAYWL QRQIGSIYPD AHIQQQKTQD ALQILSGKSL EGEDISLRDI ENDLMDLFDY
EHPEMVGKLV SNRDRIVWAT RWRRVAEDTD ARNLLEVEMV EAGQRAILNE LLGDQEAGAE
GPRPSKKMKL DLMDIDIPKA QTDSQEEKKD GALSGGLQPQ RLINLENLVF EQGNHLMTNP
KVVLPQGSTK RTFKGYEEIH VPAPKARIDP GEKLVPTTDL PDWARQGFGS AKSLNRIQSK
CYPSAFGDDG NMLVCAPTGS GKTNVAMLTM LREIGKHRNP ETGEIMLDDF KIIYIAPLKA
LVQEQVGNFG KRLESYGIRV SELTGDRQLT KQQIADTQVI VTTPEKWDVI TRKATDLSYT
RLVRLIIIDE IHLLHDDRGP VLESIVSRTI RKMEQTGDPV RIVGLSATLP NYRDVATFLR
VDPAKGLFHF DGSFRPCPLR QEFIGVTDKK AIKMLKTMND VCYAKVMEHV GTNQQQMLIF
VHSRKETAKT AKYIRDKAVE AETIGQIMRT DAASRQILQE EADQVHDANL KDLMPYGFGI
HHAGMSAADR SSVEDLFADG SLRVLVCTAT LAWGVNLPAH TVIIKGTQVY SPEKGSWVEL
SPQDVLQMLG RAGRPQYDVY GEGIIITSQA EIQYYLSLLN QQLPIESQLM SKLADNLNAE
IVLGNVQSRD QGVEWLGYTY LFVRMIRSPG LYSVGADYSN DDALEQKRVD LIHSAAVVLE
KAGLVKYDKT TGKLQATDLG RIASHYYITH HSMLTYNMHL QPSISTIELF RVFALSDEFK
YIPVRQDEKL ELAKLLGRVP IPVKEGMEEP QAKINVLLQA YISRLKLEGL ALMADLVYVT
QSAGRILRAI FEICLRKGWA SVAKVALDLC KMAEKRMWPT MTPLRQFPMC PREYIQKAER
MEVPWSSYFD LDPPRMGELL GLPKAGRVVC DLVSKFPRLE VQAQVQPMTR SMLHVELTIT
PNFVWDDALH GTAESFWIIV EDCDGEEILF HDQFILRKEF AQGDMTEHLV NFTVPISEPI
PPNYFITLVS DRWMHSETRV PVSFQKLILP ERFPPHTQLL DLQPVPVQAL KVKEYVDLYP
NWDRFNKIQT QVFKSLYDTD DSVFVGAPTG SGKTVCAEFA LLKHWKNPEA GKAVYVAPFQ
ELVDIRVADW QERLSNIGGG KTISTLTGEI TADLRILDQS DLVLATPTQW DVLSRQWQRR
KNVQNVELFI ADELHMLGGE NGAIYEVVVS RMQYIHIQLE NKMRIIGLSV PLSNARDVGE
WIGANKHTIY NFSPMARPVG LELHIQSFNI PHFPSLMMAM ARPAYQAVLQ LSPDKPAIIF
VPGRKQVRAT AVDILSACII DDDDQRFLHT NVEELAPFLE RIHERALAES LSHGIGYYHE
ALSISDKRIV SHLFKIGAIQ VMLASRDVCW EIPFTAHLVI IMGTQYFQGR EHRYVDYQIS
EILQMFGRAS RPGQDRLGKG VLMVPQVRRE YYKKFLNEAL PIESHLALSL HDAFVTEIST
KTITSTQDAV DWTTYTYFYR RLLANPSFYG LNDTSHEGLS AFLSELVETT LKELSEAKII
DLDDEDDSVS PLNPAMIAAY YNISFITMQT FLLSLTARTK LKGMLEIVTS ATEFEGIQMR
RHEDHILRRI YDRVPVKMSE PAYDSPHFKA MVLLQAHFSR MQLPIDLAKD QEVIVSKMLG
LLSACVDVLS SEGHLNAMSA MEMSQMVVQA MWDRDSPLLQ IPHFDARIVD VLARHGVKDI
DEFMTAMDPS ENPDQPKLVA EMGLTNRQLV DAANFTNSKY PSLELEFDVL EKDDVTAGSP
SYLAVKISRE TEEEEEEDDD DDDEEGGGGG GAGKGGNDEV DLTVHAPFYP AKKLENWWLV
VAEEKTRSLL AIKRVTIGKN LATKLEYVVP TPGKKDLTLF LMSDSYVGVD QSMAFSVDVA
EGMDEDEDEE DEEEEEDE
//
